[Regulation of thermal stability of enzymes by changing the composition of media. Native and modified alpha-chymotrypsin].
Stabilizing effect of denaturing salts on irreversible thermoinactivation of native and modified alpha-chymotrypsin at elevated temperatures is observed. The effect is caused by a shift of conformational equilibrium, at the primary step of reversible unfolding in the course of thermoinactivation, to a more unfolded form which is not able to refold "incorrectly". The stability of alpha-chymotrypsin is regulated within a wide range by medium alteration: the stabilizing effects are similar to those achieved by multipoint attachment of the enzyme to a support or by hydrophilization of protein by covalent modification.
Levitskiĭ
V Iu
VIu
Melik-Nubarov
N S
NS
Slepnev
V I
VI
Shikshnis
V A
VA
Mozhaev
V V
VV
D002918:Chymotrypsin / Q000378:metabolism*; D004795:Enzyme Stability; D006358:Hot Temperature; D011487:Protein Conformation; D011489:Protein Denaturation; D013050:Spectrometry, Fluorescence
D002918:Chymotrypsin
Regulirovanie termostabil'nosti fermentov izmeneniem sostava sredy. Nativnyĭ i modifitsirovannyĭ alpha-khimotripsin.